ID W6UK53_ECHGR Unreviewed; 815 AA.
AC W6UK53;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=EGR_06663 {ECO:0000313|EMBL:EUB58482.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB58482.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB58482.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000798};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB58482.1}.
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DR EMBL; APAU02000061; EUB58482.1; -; Genomic_DNA.
DR AlphaFoldDB; W6UK53; -.
DR STRING; 6210.W6UK53; -.
DR EnsemblMetazoa; XM_024495912.1; XP_024349678.1; GeneID_36342378.
DR OMA; INNAQHY; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 174..201
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 638..665
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 92301 MW; 4D708F45C2611B12 CRC64;
MSARWDCSHF LSIALRTRSK FAFIPANYDT VASWDAMVNR VQSSPEARAY TVANPFGSFA
PVRIDGQIII GIDGASYMAS VADAMEAACQ EIFIADWWLS PEIYLKRPYS DDYWRLDILL
KRKAEEGVRI CVLIYNEVKF ILNINSYHSM KTLTSLHRNI HVIRHPSHVR DRTWIWSHHE
KMVVVDQSVA FVGGIDLCFG RWDLPDHPIL DVANHRSKFE VTDLACLPLS AASLPLRLTS
FAYLEEKIGA LTNPFRLLRT DTPLPVRRSK SLNKPPLQHF PQQHKGAQRR SPSALSAGDS
TKFSGNKEAI RIRDAQRRSC CSSICPGKKE NTDRDWSFAS TETDLLASQD GNFLFPGKDY
VNWIFKDPDD VAKPDAVYID RNEVPRMPWH DAGVGLSGTI VSDFARHFIQ RWNVHRVREV
KRKRKHASTL RIPPILLPTP PHNTPLAARL HELGGSCSSG GKSARAVRMQ ALRSASHWSL
ESTRGVKAND VTTASSTSSH TECSILNAYI EAICTAQHFI YIENQFFISW VGAEKNQLVE
NQIAQAIYDR VVRAHCEKKP FRVYILIPLL AAFEGVPGDK KSGSSIHAIL RFTRTSLFKG
PNALISRLRM VIPDVENYVS VCSLRKYDCW PNGRFTTELI YIHSKLMIVD DRKMIIGSAN
INDRSMLGHR DSELAVVVED EVEEEKSGVV ADVRRRLMAE HLGVLSDQAS LPWDPALLHQ
PISDAFFHSV WRKTALDNMN IFEEVFNCVP SNSVRRYSER STQMQGKWPR GTKAAELLLG
IRGHLCEYPE DYLADEDLTF PRGNVEQLAP LKIWT
//
